Purification and physicochemical characterization of human alpha 2-HS-glycoprotein.
A large-scale purification method for alpha 2 HS-glycoprotein from normal human pooled serum is presented. 130 mg of alpha 2 HS was obtained from 21 of normal serum and the yield was 13.6%. Charge heterogeneity on isoelectrofocusing of this protein is mainly due to sialic acid. By the measurement of the circular dichroism spectrum, the alpha-helix content was calculated as 11% and the beta-structure content was calculated as 21 to 33%. alpha 2HS consists of a single polypeptide chain (Mr 49,000) of which the N-terminal amino acid is alanine. The N-terminal sequence of 31 amino acids contains 19 hydrophobic residues.
D000595:Amino Acid Sequence; D001798:Blood Proteins / Q000302:isolation & purification; D002845:Chromatography; D002942:Circular Dichroism; D004586:Electrophoresis; D005590:Fractional Precipitation; D006801:Humans; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D013056:Spectrophotometry, Ultraviolet; D060749:alpha-2-HS-Glycoprotein
C556354:AHSG protein, human; D001798:Blood Proteins; D060749:alpha-2-HS-Glycoprotein